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Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene.
Open accessAbstract
A single mutation altering the transmembrane domain of the receptor-like p185 protein encoded by the rat neu gene converts the normal neu gene into a potent oncogene. The biochemical consequences of this mutation were studied by examining phosphorylation of the normal and transforming p185 molecules in membrane preparations. Here we show that the transforming p185 is phosphorylated to a much higher extent in vitro than its normal counterpart. This preferential phosphorylation has the properties that would be expected of p185 autophosphorylation: it takes place on tyrosine and requires intact p185 kinase activity. The normal p185 protein does not demonstrate increased phosphorylation even when it coexists in a transformed cell with the transforming p185 protein. These data show that transforming p185 is specifically associated with an active tyrosine kinase activity and suggest that this activity is intrinsic to the transforming protein. Thus, the transmembrane domain of p185 appears to directly regulate its kinase activity.
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Kokai, Y., Myers, J. N., Wada, T., Brown, V. I., LeVea, C. M., Davis, J. G., Dobashi, K., & Greene, M. I. (1989) · Cell · doi:10.1016/0092-8674(89)90843-x · Cited by 309
Webster, M. K., & Donoghue, D. J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00384.x · Cited by 307
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Metadata
- Authors
- Bargmann, C. I., & Weinberg, R. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1988-08
- Volume
- 85
- Issue
- 15
- Pages
- 5394-5398
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2017213758
- Cited by
- 224
- References
- 0
- FWCI
- 8.67
- Type
- journal article
- Language
- en
- Open access
- green
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- Bargmann, C. I., & Weinberg, R. A. (1988). Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.85.15.5394
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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